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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00002570naa a2200373 4500
001oai:prod.swepub.kib.ki.se:230956813
003SwePub
008240811s2019 | |||||||||||000 ||eng|
024a http://kipublications.ki.se/Default.aspx?queryparsed=id:2309568132 URI
024a https://doi.org/10.1155/2019/65942122 DOI
040 a (SwePub)ki
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a Ochaya, S4 aut
2451 0a Characterization of Evolutionarily Conserved Trypanosoma cruzi NatC and NatA-N-Terminal Acetyltransferase Complexes
264 1b Hindawi Limited,c 2019
520 a Protein N-terminal acetylation is a co- and posttranslational modification, conserved among eukaryotes. It determines the functional fate of many proteins including their stability, complex formation, and subcellular localization. N-terminal acetyltransferases (NATs) transfer an acetyl group to the N-termini of proteins, and the major NATs in yeast and humans are NatA, NatB, and NatC. In this study, we characterized the Trypanosoma cruzi (T. cruzi) NatC and NatA protein complexes, each consisting of one catalytic subunit and predicted auxiliary subunits. The proteins were found to be expressed in the three main life cycle stages of the parasite, formed stable complexes in vivo, and partially cosedimented with the ribosome in agreement with a cotranslational function. An in vitro acetylation assay clearly demonstrated that the acetylated substrates of the NatC catalytic subunit from T. cruzi were similar to those of yeast and human NatC, suggesting evolutionary conservation of function. An RNAi knockdown of the Trypanosoma brucei (T. brucei) NatC catalytic subunit indicated that reduced NatC-mediated N-terminal acetylation of target proteins reduces parasite growth.
700a Franzén, Ou Karolinska Institutet4 aut
700a Buhwa, DA4 aut
700a Foyn, H4 aut
700a Butler, CE4 aut
700a Stove, SI4 aut
700a Tyler, KM4 aut
700a Arnesen, T4 aut
700a Matovu, E4 aut
700a Åslund, L4 aut
700a Andersson, Bu Karolinska Institutet4 aut
710a Karolinska Institutet4 org
773t Journal of parasitology researchd : Hindawi Limitedg 2019, s. 6594212-q 2019<6594212-x 2090-0023x 2090-0031
856u https://doi.org/10.1155/2019/6594212
8564 8u http://kipublications.ki.se/Default.aspx?queryparsed=id:230956813
8564 8u https://doi.org/10.1155/2019/6594212

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